1a1j
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RADR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCGT SITE)
OverviewOverview
BACKGROUND: Zinc fingers of the Cys2-His2 class comprise one of the, largest families of eukaryotic DNA-binding motifs and recognize a diverse, set of DNA sequences. These proteins have a relatively simple modular, structure and key base contacts are typically made by a few residues from, each finger. These features make the zinc finger motif an attractive, system for designing novel DNA-binding proteins and for exploring, fundamental principles of protein-DNA recognition. RESULTS: Here we report, the X-ray crystal structures of zinc finger-DNA complexes involving three, variants of Zif268, with multiple changes in the recognition helix of, finger one. We describe the structure of each of these three-finger, peptides bound to its corresponding target site. To help elucidate the, differential basis for site-specific recognition, the structures of four, other complexes containing various combinations of these peptides with, alternative binding sites have also been determined. CONCLUSIONS: The, protein-DNA contacts observed in these complexes reveal the basis for the, specificity demonstrated by these Zif268 variants. Many, but not all, of, the contacts can be rationalized in terms of a recognition code, but the, predictive value of such a code is limited. The structures illustrate how, modest changes in the docking arrangement accommodate the new, sidechain-base and sidechain-phosphate interactions. Such adaptations help, explain the versatility of naturally occurring zinc finger proteins and, their utility in design.
About this StructureAbout this Structure
1A1J is a Single protein structure of sequence from Mus musculus with ZN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
High-resolution structures of variant Zif268-DNA complexes: implications for understanding zinc finger-DNA recognition., Elrod-Erickson M, Benson TE, Pabo CO, Structure. 1998 Apr 15;6(4):451-64. PMID:9562555
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